IL6RB_MOUSE
ID IL6RB_MOUSE Reviewed; 917 AA.
AC Q00560; G5E8D2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Interleukin-6 receptor subunit beta {ECO:0000305};
DE Short=IL-6 receptor subunit beta;
DE Short=IL-6R subunit beta;
DE Short=IL-6R-beta;
DE Short=IL-6RB;
DE AltName: Full=Interleukin-6 signal transducer;
DE AltName: Full=Membrane glycoprotein 130;
DE Short=gp130 {ECO:0000303|PubMed:1602143};
DE AltName: Full=Oncostatin-M receptor subunit alpha;
DE AltName: CD_antigen=CD130;
DE Flags: Precursor;
GN Name=Il6st {ECO:0000312|MGI:MGI:96560};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=ICR; TISSUE=Macrophage;
RX PubMed=1602143;
RA Saito M., Yoshida K., Hibi M., Taga T., Kishimoto T.;
RT "Molecular cloning of a murine IL-6 receptor-associated signal transducer,
RT gp130, and its regulated expression in vivo.";
RL J. Immunol. 148:4066-4071(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8552649; DOI=10.1073/pnas.93.1.407;
RA Yoshida K., Taga T., Saito M., Suematsu S., Kumanogoh A., Tanaka T.,
RA Fujiwara H., Hirata M., Yamagami T., Nakahata T., Hirabayashi T.,
RA Yoneda Y., Tanaka K., Wang W.Z., Mori C., Shiota K., Yoshida N.,
RA Kishimoto T.;
RT "Targeted disruption of gp130, a common signal transducer for the
RT interleukin 6 family of cytokines, leads to myocardial and hematological
RT disorders.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:407-411(1996).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9348227; DOI=10.1210/endo.138.11.5534;
RA Kawasaki K., Gao Y.H., Yokose S., Kaji Y., Nakamura T., Suda T.,
RA Yoshida K., Taga T., Kishimoto T., Kataoka H., Yuasa T., Norimatsu H.,
RA Yamaguchi A.;
RT "Osteoclasts are present in gp130-deficient mice.";
RL Endocrinology 138:4959-4965(1997).
RN [6]
RP FUNCTION.
RC TISSUE=Thymus;
RX PubMed=9202125; DOI=10.1038/43206;
RA Starr R., Willson T.A., Viney E.M., Murray L.J.L., Rayner J.R.,
RA Jenkins B.J., Gonda T.J., Alexander W.S., Metcalf D., Nicola N.A.,
RA Hilton D.J.;
RT "A family of cytokine-inducible inhibitors of signaling.";
RL Nature 387:917-921(1997).
RN [7]
RP SUBUNIT.
RX PubMed=9920829;
RA Tanaka M., Hara T., Copeland N.G., Gilbert D.J., Jenkins N.A., Miyajima A.;
RT "Reconstitution of the functional mouse oncostatin M (OSM) receptor:
RT molecular cloning of the OSM receptor beta subunit.";
RL Blood 93:804-815(1999).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10377352; DOI=10.1523/jneurosci.19-13-05429.1999;
RA Nakashima K., Wiese S., Yanagisawa M., Arakawa H., Kimura N., Hisatsune T.,
RA Yoshida K., Kishimoto T., Sendtner M., Taga T.;
RT "Developmental requirement of gp130 signaling in neuronal survival and
RT astrocyte differentiation.";
RL J. Neurosci. 19:5429-5434(1999).
RN [9]
RP FUNCTION.
RX PubMed=10661409; DOI=10.1016/s1074-7613(00)80162-4;
RA Ohtani T., Ishihara K., Atsumi T., Nishida K., Kaneko Y., Miyata T.,
RA Itoh S., Narimatsu M., Maeda H., Fukada T., Itoh M., Okano H., Hibi M.,
RA Hirano T.;
RT "Dissection of signaling cascades through gp130 in vivo: reciprocal roles
RT for STAT3- and SHP2-mediated signals in immune responses.";
RL Immunity 12:95-105(2000).
RN [10]
RP INTERACTION WITH INPP5D.
RX PubMed=17105399; DOI=10.1089/scd.2006.15.641;
RA Desponts C., Ninos J.M., Kerr W.G.;
RT "s-SHIP associates with receptor complexes essential for pluripotent stem
RT cell growth and survival.";
RL Stem Cells Dev. 15:641-646(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24339143; DOI=10.1002/jbmr.2159;
RA Johnson R.W., Brennan H.J., Vrahnas C., Poulton I.J., McGregor N.E.,
RA Standal T., Walker E.C., Koh T.T., Nguyen H., Walsh N.C., Forwood M.R.,
RA Martin T.J., Sims N.A.;
RT "The primary function of gp130 signaling in osteoblasts is to maintain bone
RT formation and strength, rather than promote osteoclast formation.";
RL J. Bone Miner. Res. 29:1492-1505(2014).
RN [15]
RP FUNCTION.
RX PubMed=25228504; DOI=10.1530/joe-14-0424;
RA Standal T., Johnson R.W., McGregor N.E., Poulton I.J., Ho P.W.,
RA Martin T.J., Sims N.A.;
RT "gp130 in late osteoblasts and osteocytes is required for PTH-induced
RT osteoblast differentiation.";
RL J. Endocrinol. 223:181-190(2014).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25057188; DOI=10.1523/jneurosci.5161-13.2014;
RA Malsch P., Andratsch M., Vogl C., Link A.S., Alzheimer C., Brierley S.M.,
RA Hughes P.A., Kress M.;
RT "Deletion of interleukin-6 signal transducer gp130 in small sensory neurons
RT attenuates mechanonociception and down-regulates TRPA1 expression.";
RL J. Neurosci. 34:9845-9856(2014).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26255596; DOI=10.1016/j.bone.2015.08.005;
RA Johnson R.W., McGregor N.E., Brennan H.J., Crimeen-Irwin B., Poulton I.J.,
RA Martin T.J., Sims N.A.;
RT "Glycoprotein130 (Gp130)/interleukin-6 (IL-6) signalling in osteoclasts
RT promotes bone formation in periosteal and trabecular bone.";
RL Bone 81:343-351(2015).
RN [18]
RP FUNCTION.
RX PubMed=25731159; DOI=10.1038/nature14228;
RA Taniguchi K., Wu L.W., Grivennikov S.I., de Jong P.R., Lian I., Yu F.X.,
RA Wang K., Ho S.B., Boland B.S., Chang J.T., Sandborn W.J., Hardiman G.,
RA Raz E., Maehara Y., Yoshimura A., Zucman-Rossi J., Guan K.L., Karin M.;
RT "A gp130-Src-YAP module links inflammation to epithelial regeneration.";
RL Nature 519:57-62(2015).
RN [19]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY OBESITY.
RX PubMed=28402851; DOI=10.1016/j.celrep.2017.03.043;
RA Timper K., Denson J.L., Steculorum S.M., Heilinger C., Engstroem-Ruud L.,
RA Wunderlich C.M., Rose-John S., Wunderlich F.T., Bruening J.C.;
RT "IL-6 Improves Energy and Glucose Homeostasis in Obesity via Enhanced
RT Central IL-6 trans-Signaling.";
RL Cell Rep. 19:267-280(2017).
RN [20]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=27893700; DOI=10.1038/ni.3632;
RA Heink S., Yogev N., Garbers C., Herwerth M., Aly L., Gasperi C.,
RA Husterer V., Croxford A.L., Moeller-Hackbarth K., Bartsch H.S., Sotlar K.,
RA Krebs S., Regen T., Blum H., Hemmer B., Misgeld T., Wunderlich T.F.,
RA Hidalgo J., Oukka M., Rose-John S., Schmidt-Supprian M., Waisman A.,
RA Korn T.;
RT "Trans-presentation of IL-6 by dendritic cells is required for the priming
RT of pathogenic TH17 cells.";
RL Nat. Immunol. 18:74-85(2017).
CC -!- FUNCTION: Signal-transducing molecule (PubMed:1602143). The receptor
CC systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST
CC for initiating signal transmission. Binding of IL6 to IL6R induces
CC IL6ST homodimerization and formation of a high-affinity receptor
CC complex, which activates the intracellular JAK-MAPK and JAK-STAT3
CC signaling pathways (PubMed:1602143, PubMed:10661409). That causes
CC phosphorylation of IL6ST tyrosine residues which in turn activates
CC STAT3 (PubMed:10661409). In parallel, the IL6 signaling pathway induces
CC the expression of two cytokine receptor signaling inhibitors, SOCS1 and
CC SOCS3, which inhibit JAK and terminate the activity of the IL6
CC signaling pathway as a negative feedback loop (PubMed:9202125). Also
CC activates the yes-associated protein 1 (YAP) and NOTCH pathways to
CC control inflammation-induced epithelial regeneration, independently of
CC STAT3 (PubMed:25731159). Mediates signals which regulate immune
CC response, hematopoiesis, pain control and bone metabolism
CC (PubMed:10661409, PubMed:26255596, PubMed:25057188, PubMed:8552649).
CC Has a role in embryonic development (PubMed:10661409). Essential for
CC survival of motor and sensory neurons and for differentiation of
CC astrocytes (PubMed:10377352). Required for expression of TRPA1 in
CC nociceptive neurons (PubMed:25057188). Required for the maintenance of
CC PTH1R expression in the osteoblast lineage and for the stimulation of
CC PTH-induced osteoblast differentiation (PubMed:25228504). Required for
CC normal trabecular bone mass and cortical bone composition
CC (PubMed:24339143, PubMed:9348227, PubMed:26255596).
CC {ECO:0000250|UniProtKB:P40189, ECO:0000269|PubMed:10377352,
CC ECO:0000269|PubMed:10661409, ECO:0000269|PubMed:1602143,
CC ECO:0000269|PubMed:24339143, ECO:0000269|PubMed:25057188,
CC ECO:0000269|PubMed:25228504, ECO:0000269|PubMed:25731159,
CC ECO:0000269|PubMed:26255596, ECO:0000269|PubMed:8552649,
CC ECO:0000269|PubMed:9202125, ECO:0000269|PubMed:9348227}.
CC -!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and
CC IL6ST; associates with the complex IL6:IL6R but does not interact with
CC IL6 (By similarity). Forms heterodimers composed of LIFR and IL6ST
CC (type I OSM receptor) which are activated by LIF and OSM. Also forms
CC heterodimers composed of OSMR and IL6ST (type II receptor) which are
CC activated by OSM but not by LIF. Interacts with HCK (By similarity).
CC Interacts with INPP5D/SHIP1 (PubMed:17105399). Interacts with SRC and
CC YES (By similarity). {ECO:0000250|UniProtKB:P40189,
CC ECO:0000269|PubMed:17105399, ECO:0000269|PubMed:9920829}.
CC -!- INTERACTION:
CC Q00560; O35718: Socs3; NbExp=6; IntAct=EBI-3862992, EBI-2659360;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P40189};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expression not restricted to IL6-responsive cells.
CC Found in tissues such as brain, heart, thymus, spleen, kidney, lung and
CC liver. Found in all the cell lines tested except BaF-B03. Expressed
CC paraventricular nucleus of the hypothalamus (PubMed:28402851).
CC {ECO:0000269|PubMed:1602143, ECO:0000269|PubMed:28402851}.
CC -!- DEVELOPMENTAL STAGE: In embryonic stem cells it is found from day 6 of
CC gestation. It reaches a peak on day 8 and gradually declines during the
CC rest of embryogenesis. {ECO:0000269|PubMed:1602143}.
CC -!- INDUCTION: In paraventricular nucleus of the hypothalamus, expression
CC is enhanced by obesity. {ECO:0000269|PubMed:28402851}.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- PTM: Phosphorylation of Ser-780 down-regulates cell surface expression.
CC {ECO:0000250|UniProtKB:P40189}.
CC -!- PTM: Heavily N-glycosylated. Glycosylation is required for protein
CC stability and localization in plasma membrane but not for ligand
CC binding. {ECO:0000250|UniProtKB:P40189}.
CC -!- DISRUPTION PHENOTYPE: Progressively lethal between 12.5 dpc and birth
CC (PubMed:8552649). Embryos show hypoplastic ventricular myocardium
CC without septal and trabecular defect, reduced numbers of pluripotential
CC and committed hematopoietic progenitors in liver and reduced
CC differentiated lineages in thymus (PubMed:8552649). Impaired
CC differentiation of astrocytes and decreased number of dorsal root
CC ganglion and motor neurons at 18.5 dpc (PubMed:10377352). Decreased
CC volume of mineralized trabecular bones, while number of osteoclasts is
CC increased (PubMed:9348227, PubMed:26255596). Conditional knockout from
CC the entire osteoblast lineage or specifically in osteocytes causes no
CC significant skeletal or morphological defects but mice show 30% lower
CC trabecular bone formation rate and larger cortical diameter compared to
CC wild type (PubMed:24339143, PubMed:26255596). Conditional knockout in
CC primary nociceptive afferents causes reduced sensitivity to mechanical
CC stimulation due to reduced sensitivity of nociceptive neurons and
CC reduces TRPA1 mRNA expression in dorsal root ganglion neurons
CC (PubMed:25057188). {ECO:0000269|PubMed:10377352,
CC ECO:0000269|PubMed:24339143, ECO:0000269|PubMed:25057188,
CC ECO:0000269|PubMed:26255596, ECO:0000269|PubMed:8552649,
CC ECO:0000269|PubMed:9348227}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; X62646; CAA44515.1; -; mRNA.
DR EMBL; M83336; AAA37723.1; -; mRNA.
DR EMBL; AC159196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466568; EDL18412.1; -; Genomic_DNA.
DR CCDS; CCDS26773.1; -.
DR PIR; I49699; I49699.
DR RefSeq; NP_034690.3; NM_010560.3.
DR PDB; 2BBU; NMR; -; B=750-764.
DR PDB; 2HMH; X-ray; 2.00 A; B=753-763.
DR PDB; 4GL9; X-ray; 3.90 A; I/J/K/L=750-764.
DR PDB; 6C5X; X-ray; 3.10 A; G=754-763.
DR PDBsum; 2BBU; -.
DR PDBsum; 2HMH; -.
DR PDBsum; 4GL9; -.
DR PDBsum; 6C5X; -.
DR AlphaFoldDB; Q00560; -.
DR SMR; Q00560; -.
DR BioGRID; 200643; 13.
DR CORUM; Q00560; -.
DR DIP; DIP-5782N; -.
DR IntAct; Q00560; 7.
DR STRING; 10090.ENSMUSP00000138836; -.
DR GlyConnect; 2412; 2 N-Linked glycans (1 site).
DR GlyGen; Q00560; 9 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q00560; -.
DR PhosphoSitePlus; Q00560; -.
DR SwissPalm; Q00560; -.
DR jPOST; Q00560; -.
DR MaxQB; Q00560; -.
DR PaxDb; Q00560; -.
DR PRIDE; Q00560; -.
DR ProteomicsDB; 269398; -.
DR Antibodypedia; 2448; 813 antibodies from 39 providers.
DR DNASU; 16195; -.
DR Ensembl; ENSMUST00000070731; ENSMUSP00000064205; ENSMUSG00000021756.
DR Ensembl; ENSMUST00000183663; ENSMUSP00000138836; ENSMUSG00000021756.
DR Ensembl; ENSMUST00000184311; ENSMUSP00000139227; ENSMUSG00000021756.
DR GeneID; 16195; -.
DR KEGG; mmu:16195; -.
DR UCSC; uc007rwg.2; mouse.
DR CTD; 3572; -.
DR MGI; MGI:96560; Il6st.
DR VEuPathDB; HostDB:ENSMUSG00000021756; -.
DR eggNOG; ENOG502QXEG; Eukaryota.
DR GeneTree; ENSGT00940000159608; -.
DR InParanoid; Q00560; -.
DR OMA; KPNPPRN; -.
DR OrthoDB; 144839at2759; -.
DR PhylomeDB; Q00560; -.
DR TreeFam; TF338122; -.
DR Reactome; R-MMU-1059683; Interleukin-6 signaling.
DR Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
DR Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
DR Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-MMU-8984722; Interleukin-35 Signalling.
DR Reactome; R-MMU-9020956; Interleukin-27 signaling.
DR BioGRID-ORCS; 16195; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Il6st; mouse.
DR EvolutionaryTrace; Q00560; -.
DR PRO; PR:Q00560; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q00560; protein.
DR Bgee; ENSMUSG00000021756; Expressed in decidua and 259 other tissues.
DR ExpressionAtlas; Q00560; baseline and differential.
DR Genevisible; Q00560; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005896; C:interleukin-6 receptor complex; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR GO; GO:0005900; C:oncostatin-M receptor complex; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; ISO:MGI.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:MGI.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019970; F:interleukin-11 binding; IDA:MGI.
DR GO; GO:0004921; F:interleukin-11 receptor activity; IDA:MGI.
DR GO; GO:0019981; F:interleukin-6 binding; ISO:MGI.
DR GO; GO:0004915; F:interleukin-6 receptor activity; ISO:MGI.
DR GO; GO:0005138; F:interleukin-6 receptor binding; ISO:MGI.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; ISO:MGI.
DR GO; GO:0004924; F:oncostatin-M receptor activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:MGI.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0060576; P:intestinal epithelial cell development; IDA:UniProtKB.
DR GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; ISO:MGI.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0070104; P:negative regulation of interleukin-6-mediated signaling pathway; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:MGI.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IDA:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR GO; GO:0006642; P:triglyceride mobilization; ISO:MGI.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 6.
DR IDEAL; IID50222; -.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR010457; IgC2-like_lig-bd.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR Pfam; PF06328; Lep_receptor_Ig; 1.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..917
FT /note="Interleukin-6 receptor subunit beta"
FT /id="PRO_0000010900"
FT TOPO_DOM 23..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..917
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..120
FT /note="Ig-like C2-type"
FT DOMAIN 128..221
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 222..322
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 327..417
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 422..515
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 517..611
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 658..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 308..312
FT /note="WSXWS motif"
FT MOTIF 649..657
FT /note="Box 1 motif"
FT COMPBIAS 722..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..54
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT DISULFID 48..103
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT DISULFID 134..144
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT DISULFID 172..180
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT DISULFID 456..464
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT CONFLICT 756
FT /note="Q -> E (in Ref. 1; CAA44515/AAA37723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 917 AA; 102451 MW; EDA69AB865E5A6E8 CRC64;
MSAPRIWLAQ ALLFFLTTES IGQLLEPCGY IYPEFPVVQR GSNFTAICVL KEACLQHYYV
NASYIVWKTN HAAVPREQVT VINRTTSSVT FTDVVLPSVQ LTCNILSFGQ IEQNVYGVTM
LSGFPPDKPT NLTCIVNEGK NMLCQWDPGR ETYLETNYTL KSEWATEKFP DCQSKHGTSC
MVSYMPTYYV NIEVWVEAEN ALGKVSSESI NFDPVDKVKP TPPYNLSVTN SEELSSILKL
SWVSSGLGGL LDLKSDIQYR TKDASTWIQV PLEDTMSPRT SFTVQDLKPF TEYVFRIRSI
KDSGKGYWSD WSEEASGTTY EDRPSRPPSF WYKTNPSHGQ EYRSVRLIWK ALPLSEANGK
ILDYEVILTQ SKSVSQTYTV TGTELTVNLT NDRYVASLAA RNKVGKSAAA VLTIPSPHVT
AAYSVVNLKA FPKDNLLWVE WTPPPKPVSK YILEWCVLSE NAPCVEDWQQ EDATVNRTHL
RGRLLESKCY QITVTPVFAT GPGGSESLKA YLKQAAPARG PTVRTKKVGK NEAVLAWDQI
PVDDQNGFIR NYSISYRTSV GKEMVVHVDS SHTEYTLSSL SSDTLYMVRM AAYTDEGGKD
GPEFTFTTPK FAQGEIEAIV VPVCLAFLLT TLLGVLFCFN KRDLIKKHIW PNVPDPSKSH
IAQWSPHTPP RHNFNSKDQM YSDGNFTDVS VVEIEANNKK PCPDDLKSVD LFKKEKVSTE
GHSSGIGGSS CMSSSRPSIS SNEENESAQS TASTVQYSTV VHSGYRHQVP SVQVFSRSES
TQPLLDSEER PEDLQLVDSV DGGDEILPRQ PYFKQNCSQP EACPEISHFE RSNQVLSGNE
EDFVRLKQQQ VSDHISQPYG SEQRRLFQEG STADALGTGA DGQMERFESV GMETTIDEEI
PKSYLPQTVR QGGYMPQ
